3a7e
From Proteopedia
(Difference between revisions)
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3a7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a7e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3a7e RCSB], [http://www.ebi.ac.uk/pdbsum/3a7e PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3a7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a7e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3a7e RCSB], [http://www.ebi.ac.uk/pdbsum/3a7e PDBsum]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/COMT_HUMAN COMT_HUMAN]] Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
+ | |||
+ | ==See Also== | ||
+ | *[[Catechol O-methyltransferase|Catechol O-methyltransferase]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Catechol O-methyltransferase]] | [[Category: Catechol O-methyltransferase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: Tsuji, E | + | [[Category: Tsuji, E]] |
[[Category: Alternative initiation]] | [[Category: Alternative initiation]] | ||
[[Category: Catecholamine metabolism]] | [[Category: Catecholamine metabolism]] |
Revision as of 19:57, 25 December 2014
Crystal structure of human COMT complexed with SAM and 3,5-dinitrocatechol
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Categories: Catechol O-methyltransferase | Homo sapiens | Tsuji, E | Alternative initiation | Catecholamine metabolism | Cell membrane | Comt | Magnesium | Membrane | Metal-binding | Methyltransferase | Neurotransmitter degradation | Phosphoprotein | S-adenosyl-l-methionine | Signal-anchor | Transferase | Transmembrane